A novel preparative method for the isolation of avidin and riboflavin-binding glycoprotein from chicken egg-white by the use of high-performance liquid chromatography.
A method for the rapid preparative isolation of highly purified avidin using h.p.l.c. on a powerful cation-exchanger TSK SP-5PW column has been developed. The method is based on the following properties of avidin: solubility at a high (NH4)2SO4 concentration, stability and relatively low solubility in organic solvents, as well as the strongly cationic nature of the molecule. Riboflavin-binding glycoprotein may be isolated as by-product.
Piskarev
V E
VE
N.D. Zelinsky Institute of Organic Chemistry, Academy of Sciences of the U.S.S.R., Moscow.
Shuster
A M
AM
Gabibov
A G
AG
Rabinkov
A G
AG
D000818:Animals; D001360:Avidin / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000302:isolation & purification*; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004529:Egg White / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D026901:Membrane Transport Proteins; D013056:Spectrophotometry, Ultraviolet
D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D001360:Avidin